Manganese in PDB 1lzi: Glycosyltransferase A + Udp + H Antigen Acceptor

All present enzymatic activity of Glycosyltransferase A + Udp + H Antigen Acceptor:
2.4.1.40;

The structure of Glycosyltransferase A + Udp + H Antigen Acceptor, PDB code: 1lzi was solved by S.I.Patenaude, N.O.L.Seto, S.N.Borisova, A.Szpacenko, S.L.Marcus, M.M.Palcic, S.V.Evans, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.35
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	52.810, 149.580, 79.970, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 20

The structure of Glycosyltransferase A + Udp + H Antigen Acceptor also contains other interesting chemical elements:

Mercury

(Hg)

5 atoms

The binding sites of Manganese atom in the Glycosyltransferase A + Udp + H Antigen Acceptor (pdb code 1lzi). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Glycosyltransferase A + Udp + H Antigen Acceptor, PDB code: 1lzi:

Manganese binding site 1 out of 1 in the Glycosyltransferase A + Udp + H Antigen Acceptor


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Glycosyltransferase A + Udp + H Antigen Acceptor within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn406 b:32.1 occ:1.00 O1A A:UDP475 2.2 49.8 1.0 O1B A:UDP475 2.3 49.9 1.0 OD2 A:ASP213 2.4 17.3 1.0 OD1 A:ASP213 2.8 21.9 1.0 CG A:ASP213 3.0 15.8 1.0 O A:HOH847 3.1 38.4 1.0 OD2 A:ASP211 3.3 23.3 1.0 PA A:UDP475 3.3 48.2 1.0 O3A A:UDP475 3.4 49.6 1.0 PB A:UDP475 3.4 50.1 1.0 CG A:ASP211 3.5 17.8 1.0 CB A:ASP211 3.7 14.2 1.0 O3' A:UDP475 3.8 46.1 1.0 O3B A:UDP475 3.8 50.7 1.0 O A:HOH648 4.0 32.0 1.0 O5' A:UDP475 4.2 47.9 1.0 OD1 A:ASP211 4.3 17.7 1.0 O A:HOH787 4.4 34.9 1.0 C5' A:UDP475 4.4 46.8 1.0 C3' A:UDP475 4.5 46.8 1.0 CB A:ASP213 4.5 15.2 1.0 O2A A:UDP475 4.5 49.5 1.0 O2B A:UDP475 4.7 50.6 1.0 O A:HOH669 4.7 29.2 1.0 O A:ASP213 4.9 14.3 1.0 C4' A:UDP475 4.9 46.7 1.0

S.I.Patenaude, N.O.Seto, S.N.Borisova, A.Szpacenko, S.L.Marcus, M.M.Palcic, S.V.Evans. The Structural Basis For Specificity in Human Abo(H) Blood Group Biosynthesis. Nat.Struct.Biol. V. 9 685 2002.
ISSN: ISSN 1072-8368
PubMed: 12198488
DOI: 10.1038/NSB832